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Analyzing Large Protein Complexes by Structural Mass Spectrometry
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A structural model of the immune checkpoint CD160-HVEM complex derived from HDX-mass spectrometry and molecular

Katarzyna Kuncewicz1, Marta Spodzieja1, Adam Sieradzan2

  • 1University of Gdansk, Faculty of Chemistry, Department of Biomedical Chemistry, Gdansk, Poland.

Oncotarget
|February 8, 2019
PubMed

Insights

Researchers mapped the 3D structure of the CD160-HVEM complex, crucial for T cell regulation. This finding advances understanding of immune responses and aids in developing new immunotherapies.

Area of Science:

  • Immunology
  • Structural Biology
  • Molecular Biology

Background:

  • CD160 is a T cell coinhibitory molecule.
  • It interacts with herpes virus entry mediator (HVEM) on antigen-presenting cells.
  • The structure of CD160 and its complex with HVEM were previously unknown.

Purpose of the Study:

  • To determine the molecular structure of the CD160-HVEM complex.
  • To provide insights into the tertiary structure of CD160.
  • To lay the groundwork for designing novel immunotherapies.

Main Methods:

  • Enzyme-linked immunosorbent assay (ELISA)
  • Hydrogen/deuterium exchange mass spectrometry (HDX-MS)
  • Affinity chromatography
  • Mass spectrometry (MS)

Main Results:

  • Identified CD160 fragments interacting with HVEM.
  • Obtained key information on CD160's tertiary structure using HDX-MS.
  • Predicted the 3D structure of the CD160-HVEM complex.

Conclusions:

  • The study reveals the molecular architecture of the CD160-HVEM complex.
  • This structural information is vital for developing inhibitors for future immunotherapies.
  • Understanding this interaction can modulate T cell responses.

Keywords:
CD160HVEMhydrogen/deuterium exchange combined to mass spectrometryimmune checkpointsmolecular modeling

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